Outer membrane beta-barrels are folded and inserted into the outer membrane by the Bam complex (BamABCDE).

We have purified the protein components of the Bam complex and reconstituted beta-barrel assembly activity in vitro. However, the mechanism by which the Bam complex binds, folds, and inserts its substrates into the outer membrane remains unclear. Our lab uses in vitro and in vivo biochemical tools to characterize the molecular mechanism of beta-barrel assembly. One method we use is the generation of substrates that stall during their assembly, which allows us to probe their interactions with the Bam complex. Our long-term goal is to use mechanistic information we obtain to develop ways of inhibiting the Bam complex as a means of targeting pathogenic Gram-negative bacteria.